SPECIFICITY AND LIPID BINDING SITE OF BOVINE PHOSPHATIDYLCHOLINE TRANSFER PROTEIN

1983 ◽  
pp. 253-264
Author(s):  
Karel W. A. Wirtz ◽  
Robert Akeroyd ◽  
Jan Westerman ◽  
Laurens L. M. van Deenen
Keyword(s):  
Binding Site ◽  
Lipid Binding ◽  
Transfer Protein ◽  
Phosphatidylcholine Transfer Protein ◽  
Lipid Binding Site

Identification of the Lipid-Binding Site of Phosphatidylcholine-Transfer Protein with Phosphatidylcholine Analogs Containing Photactivable Carbene Precursors

1983 ◽  
Vol 132 (2) ◽  
pp. 441-449 ◽  
Author(s):  
Jan WESTERMAN ◽  
Karel W. A. WIRTZ ◽  
Theo BERKHOUT ◽  
Laurens L. M. DEENEN ◽  
Ramachandran RADHAKRISHNAN ◽  
...  
Keyword(s):  
Binding Site ◽  
Lipid Binding ◽  
Transfer Protein ◽  
Phosphatidylcholine Transfer Protein ◽  
Lipid Binding Site

scholarly journals Elucidation of the anti-autophagy mechanism of the Legionella effector RavZ using semisynthetic LC3 proteins

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Aimin Yang ◽  
Supansa Pantoom ◽  
Yao-Wen Wu
Keyword(s):  
Legionella Pneumophila ◽  
Lipid Binding ◽  
Effector Protein ◽  
Intracellular Pathogen ◽  
Transfer Protein ◽  
Phospholipid Transfer ◽  
Acyl Chains ◽  
Pathogenic Microbes ◽  
Lir Motif ◽  
Lipid Binding Site

Autophagy is a conserved cellular process involved in the elimination of proteins and organelles. It is also used to combat infection with pathogenic microbes. The intracellular pathogen Legionella pneumophila manipulates autophagy by delivering the effector protein RavZ to deconjugate Atg8/LC3 proteins coupled to phosphatidylethanolamine (PE) on autophagosomal membranes. To understand how RavZ recognizes and deconjugates LC3-PE, we prepared semisynthetic LC3 proteins and elucidated the structures of the RavZ:LC3 interaction. Semisynthetic LC3 proteins allowed the analysis of structure-function relationships. RavZ extracts LC3-PE from the membrane before deconjugation. RavZ initially recognizes the LC3 molecule on membranes via its N-terminal LC3-interacting region (LIR) motif. The RavZ α3 helix is involved in extraction of the PE moiety and docking of the acyl chains into the lipid-binding site of RavZ that is related in structure to that of the phospholipid transfer protein Sec14. Thus, Legionella has evolved a novel mechanism to specifically evade host autophagy.

The N-Terminus is the Lipid-Binding Site of SAA: Supporting Evidence by MoAbs

1991 ◽  
pp. 83-86
Author(s):  
Yifat Ziq-Bachar ◽  
David Levartowsky ◽  
Mordechaipras ◽  
Alistair F. Strachan ◽  
Mati Fridkin ◽  
...  
Keyword(s):  
Binding Site ◽  
Lipid Binding ◽  
Supporting Evidence ◽  
N Terminus ◽  
Lipid Binding Site

scholarly journals Phospholipid-induced structural changes to an erythroid β spectrin ankyrin-dependent lipid-binding site

2008 ◽  
Vol 1778 (11) ◽  
pp. 2612-2620 ◽  
Author(s):  
Aleksander Czogalla ◽  
Krzysztof Grzymajło ◽  
Adam Jezierski ◽  
Aleksander F. Sikorski
Keyword(s):  
Binding Site ◽  
Structural Changes ◽  
Lipid Binding ◽  
Lipid Binding Site

scholarly journals Human TRPC5 structures reveal interaction of a xanthine-based TRPC1/4/5 inhibitor with a conserved lipid binding site

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
David J. Wright ◽  
Katie J. Simmons ◽  
Rachel M. Johnson ◽  
David J. Beech ◽  
Stephen P. Muench ◽  
...  
Keyword(s):  
Binding Site ◽  
Lipid Binding ◽  
Structural Basis ◽  
Chemical Probes ◽  
Endogenous Factors ◽  
Drug Candidates ◽  
Channel Regulation ◽  
Exogenous Factors ◽  
Translational Studies ◽  
Lipid Binding Site

AbstractTRPC1/4/5 channels are non-specific cation channels implicated in a wide variety of diseases, and TRPC1/4/5 inhibitors have recently entered clinical trials. However, fundamental and translational studies require a better understanding of TRPC1/4/5 channel regulation by endogenous and exogenous factors. Although several potent and selective TRPC1/4/5 modulators have been reported, the paucity of mechanistic insights into their modes-of-action remains a barrier to the development of new chemical probes and drug candidates. Xanthine-based modulators include the most potent and selective TRPC1/4/5 inhibitors described to date, as well as TRPC5 activators. Our previous studies suggest that xanthines interact with a, so far, elusive pocket of TRPC1/4/5 channels that is essential to channel gating. Here we report the structure of a small-molecule-bound TRPC1/4/5 channel—human TRPC5 in complex with the xanthine Pico145—to 3.0 Å. We found that Pico145 binds to a conserved lipid binding site of TRPC5, where it displaces a bound phospholipid. Our findings explain the mode-of-action of xanthine-based TRPC1/4/5 modulators, and suggest a structural basis for TRPC1/4/5 modulation by endogenous factors such as (phospho)lipids and Zn2+ ions. These studies lay the foundations for the structure-based design of new generations of TRPC1/4/5 modulators.

scholarly journals The Interfacial Lipid Binding Site on the Potassium Channel KcsA Is Specific for Anionic Phospholipids

2005 ◽  
Vol 89 (6) ◽  
pp. 4081-4089 ◽  
Author(s):  
Phedra Marius ◽  
Simon J. Alvis ◽  
J. Malcolm East ◽  
Anthony G. Lee
Keyword(s):  
Potassium Channel ◽  
Binding Site ◽  
Lipid Binding ◽  
Anionic Phospholipids ◽  
Potassium Channel Kcsa ◽  
Lipid Binding Site

scholarly journals 1-Oleoyl-2-acetylglycerol Stimulates 5-Lipoxygenase Activity via a Putative (Phospho)lipid Binding Site within the N-terminal C2-like Domain

2005 ◽  
Vol 280 (29) ◽  
pp. 26913-26921 ◽  
Author(s):  
Christina Hörnig ◽  
Dana Albert ◽  
Lutz Fischer ◽  
Michael Hörnig ◽  
Olof Rådmark ◽  
...  
Keyword(s):  
Binding Site ◽  
Lipid Binding ◽  
Lipoxygenase Activity ◽  
Phospho Lipid ◽  
Lipid Binding Site
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